ID A0A840MSH8_9PROT Unreviewed; 771 AA.
AC A0A840MSH8;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 18-JUN-2025, entry version 17.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00044770};
DE EC=2.4.99.28 {ECO:0000256|ARBA:ARBA00044770};
GN ORFNames=HNQ59_003347 {ECO:0000313|EMBL:MBB5020039.1};
OS Chitinivorax tropicus.
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; Chitinivorax.
OX NCBI_TaxID=714531 {ECO:0000313|EMBL:MBB5020039.1, ECO:0000313|Proteomes:UP000575898};
RN [1] {ECO:0000313|EMBL:MBB5020039.1, ECO:0000313|Proteomes:UP000575898}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27165 {ECO:0000313|EMBL:MBB5020039.1,
RC ECO:0000313|Proteomes:UP000575898};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
CC Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-
CC (1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-
CC cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-
CC D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans,octa-cis-undecaprenyl
CC diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+);
CC Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033,
CC ChEBI:CHEBI:78435; EC=2.4.99.28;
CC Evidence={ECO:0000256|ARBA:ARBA00049902};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the transpeptidase
CC family. {ECO:0000256|ARBA:ARBA00007090}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 51 family. {ECO:0000256|ARBA:ARBA00007739}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:MBB5020039.1}.
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DR EMBL; JACHHY010000023; MBB5020039.1; -; Genomic_DNA.
DR RefSeq; WP_184041448.1; NZ_JACHHY010000023.1.
DR AlphaFoldDB; A0A840MSH8; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000575898; Unassembled WGS sequence.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:TreeGrafter.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:InterPro.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3810.10; Biosynthetic peptidoglycan transglycosylase-like; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR050396; Glycosyltr_51/Transpeptidase.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR011815; PBP_1c.
DR InterPro; IPR009647; PBP_C.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR NCBIfam; TIGR02073; PBP_1c; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF15; PENICILLIN-BINDING PROTEIN 1C; 1.
DR Pfam; PF06832; BiPBP_C; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000313|EMBL:MBB5020039.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022670};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000575898};
KW Transferase {ECO:0000313|EMBL:MBB5020039.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 52..216
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 300..518
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 679..766
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
FT REGION 665..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 771 AA; 85434 MW; 012E06295195371E CRC64;
MLLKRFLRML AGLLFALAIL RLWPHEPLRS FAPESAAIWS HDGELLRLTL AADQQYRLWT
PLEQISPRMI EAVKVQEDRW FDWHPGVNPV SILRGAFRTY AQEDRQGGST LSMQLVRMIH
QLNTRNPAGK LKQIGLALWL EARYSKHDIL EAYLNLVPYG RNLQGVGAAS LTYFGKTPDK
LSLPEAITLA VIPQHPNLRA DRLLGAPRLQ KARLRVLSRW PARWPLGEAE RQLARQPLPL
RPLSSLPFLA PHFVDSLLLD QPGLTGPIQT TLEHRLQRLM ERQIAGYLQE KASQGVHNAA
ALLIDTRDQG VRAMIGSANY FNAAIDGQVN GTQAKRSPGS ALKPFIFGMG LDQGILHPMT
MLRDTPSAFG PFSPENFDGR FMGPISAKDA LIRSRNIPAV WVASQLKRPS LYDFLRSAGI
TQLKSEQHYG LALVLGGGEI TMEELAGLYT MLANHGELKP LRYLTSQTRP QHSPSLLSPQ
AAYLTLDMLS ANPRPDGAVL DSRHHWPIAW KTGTSWGFRD AWTVGVAGPY VLAVWLGNFN
GEGNPAFVGI DLAAPLFHRI TDALNLAEQA SPFTGWAPPA GIKQVTVCTA SGDLPNAWCP
NKTSTWFIPG KSPIRVSTLH RPVAIDNRSG RPACPPFDPA TTHLEVFEFW SSDMLKLFRE
AGIPRRTPPR PAQCDTPLAN EEGDPPRITS PLTNVTYKLS QQQAEQRIAL QATTAAGVKE
LYWFANQSFI GKAPVGQALP WRPEQGGWYG LLAVDDHGRS TSRDVKVEIA R
//
